5ul8: Difference between revisions
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<StructureSection load='5ul8' size='340' side='right'caption='[[5ul8]], [[Resolution|resolution]] 1.15Å' scene=''> | <StructureSection load='5ul8' size='340' side='right'caption='[[5ul8]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ul8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ul8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UL8 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ul8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ul8 OCA], [https://pdbe.org/5ul8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ul8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ul8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ul8 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/BLKPC_KLEPN BLKPC_KLEPN] Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Klebsiella pneumoniae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chen | [[Category: Chen Y]] | ||
[[Category: Pemberton | [[Category: Pemberton OA]] | ||
Latest revision as of 12:28, 23 October 2024
Apo KPC-2 beta-lactamase crystal structure at 1.15 Angstrom resolutionApo KPC-2 beta-lactamase crystal structure at 1.15 Angstrom resolution
Structural highlights
FunctionBLKPC_KLEPN Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency. Publication Abstract from PubMedCarbapenem-resistant Enterobacteriaceae are resistant to most beta-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A beta-lactamase. Here, we present the first product complex crystal structures of KPC-2 with beta-lactam antibiotics containing hydrolyzed cefotaxime and faropenem. They provide experimental insights into substrate recognition by KPC-2 and its unique cephalosporinase/carbapenemase activity. These structures also represent the first product complexes for a wild-type serine beta-lactamase, elucidating the product release mechanism of these enzymes in general. Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).,Pemberton OA, Zhang X, Chen Y J Med Chem. 2017 Apr 17. doi: 10.1021/acs.jmedchem.7b00158. PMID:28388065[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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